We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00774Oxysterol-binding protein family signature
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00774
Description
A number of eukaryotic proteins that seem to be involved with sterol synthesis and/or its regulation have been found [1] to be evolutionary related:
- Mammalian oxysterol-binding protein (OSBP). A protein of about 800 amino- acid residues that binds a variety of oxysterols: oxygenated derivatives of cholesterol. OSBP seems to play a complex role in the regulation of sterol metabolism.
- Mammalian OSBP-related proteins 1 to 11.
- Yeast proteins HES1 and KES1; highly related proteins of 434 residues that seem to play a role in ergosterol synthesis.
- Yeast OSH1 to OSH7.
All these proteins contain a moderately conserved domain of about 250 residues located in the C-terminal half of OBSP, OSH1 and YHR073w and in the central section of the other proteins. As a signature pattern, we selected the best conserved part of this domain, a region that contains a conserved pentapeptide.
Last update:April 2006 / Pattern revised.
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Technical section
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Reference
| 1 | Authors | Jiang B. Brown J.L. Sheraton J. Fortin N. Bussey H. |
| Title | A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein. | |
| Source | Yeast 10:341-353(1994). | |
| PubMed ID | 8017104 |
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